Disease relevance of LALBA

• The sensitization was measured (1) by systemic IgG1 antibodies directed against bovine or caprine beta-lactoglobulin (beta-lg), alpha-lactalbumin (alpha-la) and whole caseins, and (2) by intestinal anaphylaxis measured in vitro in Ussing chambers, by the rise in short-circuit current (delta Isc) in response to milk proteins [1].
• Weight gain of piglets suckling alpha-lactalbumin gilts was greater (days 7-21 after parturition) than that of control piglets [2].

High impact information on LALBA

• Neither high concentrations of N-acetylglucosamine (200 mM) nor alpha-lactalbumin inhibits the incorporation of galactose into galactosyl-beta 1,4-N-acetylglucosamine by this enzyme [3].
• About 80% of the total disaccharide synthesized at 200 mM N-acetylglucosamine was base-labile suggesting the 1,3-linkage, alpha-Lactalbumin inhibits galactose incorporation into galactosyl-beta 1,4-N-acetylglucosamine but has little or no effect on the activity of the 1,3-galactosyltransferase [4].
• Like the A state, the TFE state of alpha-lactalbumin shows little chemical shift dispersion of side-chain resonances [5].
• Taking account of the thermal unfolding of each alpha-lactalbumin, the hydrogen exchange rates of the individual tryptophan residues are analyzed [6].
• Kinetic parameters for lactose biosynthesis show absolutely no difference between the apo or Zn(II) and Ca(II) forms of alpha-lactalbumin [7].

Biological context of LALBA

• A distinct zinc binding site has been found in several alpha-lactalbumin species: bovine, human, guinea pig, and rabbit [7].
• The mutation sites (Thr29, Ala30 and Thr33) have been chosen on the basis of comparison of the amino acid sequences of goat, bovine and gunea pig alpha-lactalbumin, in which the guinea pig protein shows a remarkably more stable molten globule than the other proteins [8].
• Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state [8].
• alpha-Lactalbumin species variation, HAMLET formation, and tumor cell death [9].
• The alpha-lactalbumin transgenes were transmitted through meiosis to the sexual progeny of the regenerated plants [10].

Anatomical context of LALBA

• 1. The major milk proteins synthesized by the lactating mammary gland of the guinea pig were identified and designated as caseins A, B and C and alpha-lactalbumin, with estimated mol.wts. of 28000, 25500, 20500 and 14500 respectively [11].
• Hypotheses that 1) basal P(s) properties and 2) P(s) responses to vasoactive stimuli are sex independent were evaluated from measures of P(s) to two hydrophilic proteins, alpha-lactalbumin and porcine serum albumin (PSA), in arterioles and venules isolated from hearts of adult male and female pigs [12].
• HAMLET (human alpha-lactalbumin made lethal to tumor cells) is a tumoricidal complex of apo alpha-lactalbumin and oleic acid, formed in casein after low pH treatment of human milk [9].
• Polyadenylated RNAs isolated from bound polysomes of a lactating sow's mammary gland, were translated in a cell-free system and in vitro synthesized alpha-lactalbumin was immunoprecipitated and radiosequenced [13].
• METHODS: Segments from jejunum, ileum, colon, and rectum were mounted in Ussing diffusion chambers, and the mucosa-to-serosa passage of 14C-mannitol, fluorescein isothiocyanate (FITC)-dextran 4,400, alpha-lactalbumin, ovalbumin, and FITC-dextran 70,000 was studied [14].

Associations of LALBA with chemical compounds

• While either conformer of alpha-lactalbumin [Ca(II) or Zn(II)] is kinetically equivalent, the Ca(II) form probably dominates under physiological conditions [7].
• This was not explained by alpha-lactalbumin sequence variation, as purified bovine, equine, porcine, and caprine alpha-lactalbumins formed complexes with oleic acid with biological activity similar to HAMLET [9].
• This study examined if HAMLET-like complexes are present in casein from different species and if isolated alpha-lactalbumin from those species can form such complexes with oleic acid [9].
• Examples given are for peptides from a digest of methionine growth hormone, protein separations from whey proteins containing alpha-lactalbumin and the beta-lactoglobulins A and B, and bovine and porcine insulins [15].
• Identification of the epsilon-(gamma-glutamyl)lysine cross-linking sites in alpha-lactalbumin polymerized by mammalian and microbial transglutaminases [16].

Other interactions of LALBA

• An indirect double-antibody enzyme-linked immunosorbent assay (ELISA) was developed for the measurement of human immunoglobulin E (IgE) and IgG to the cow's milk proteins (CMP) alpha-casein, alpha-lactalbumin, and beta-lactoglobulin [17].
• Protein gamma-radiolysis in frozen solutions is a macromolecular surface phenomenon: fragmentation of lysozyme, citrate synthase and alpha-lactalbumin in native or denatured states [18].
• Prolactin increased alpha-lactalbumin accumulation to a similar extent alone, or in the presence of insulin and/or corticosterone [19].

Analytical, diagnostic and therapeutic context of LALBA

• Addition of trifluoroethanol (TFE) to bovine, human and guinea pig alpha-lactalbumin at pH 2.0 has been found in each case to induce a conformational transition in the A state as monitored by circular dichroism, nuclear magnetic resonance chemical shifts, and 1-anilinonaphthalene-8-sulphonate binding [5].
• This interaction is specific for non-native domains since native alpha-lactalbumin fails to interact with Hip. Fluorescence-anisotropy measurements indicate that reduced, carboxymethylated lactalbumin binds Hip with a Kd of 5 microM [20].
• The binding ability of alpha-lactalbumin from different species (cow, goat, giraffe, horse, pig, human, monkey, and guinea pig) was examined by a competitive radioimmunoassay [21].
• Protein dissection enhances the amyloidogenic properties of alpha-lactalbumin [22].
• Antibodies prepared against these peptides precipitate newly synthesized and secreted alpha-lactalbumin from organ cultures of mid-pregnancy mammary glands [23].

References